Zinc in PDB 1a8t: Metallo-Beta-Lactamase in Complex with L-159,061

All present enzymatic activity of Metallo-Beta-Lactamase in Complex with L-159,061:
3.5.2.6;

The structure of Metallo-Beta-Lactamase in Complex with L-159,061, PDB code: 1a8t was solved by P.M.D.Fitzgerald, J.H.Toney, N.Grover, D.Vanderwall, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.360, 170.230, 40.660, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the Metallo-Beta-Lactamase in Complex with L-159,061 (pdb code 1a8t). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Metallo-Beta-Lactamase in Complex with L-159,061, PDB code: 1a8t:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Metallo-Beta-Lactamase in Complex with L-159,061


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo-Beta-Lactamase in Complex with L-159,061 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn251 b:2.0 occ:1.00 ND1 A:HIS84 2.1 2.0 1.0 NE2 A:HIS145 2.1 2.0 1.0 NE2 A:HIS82 2.3 2.0 1.0 ZN A:ZN252 2.8 7.4 1.0 CE1 A:HIS84 3.0 2.0 1.0 CD2 A:HIS145 3.0 2.0 1.0 CD2 A:HIS82 3.0 2.0 1.0 CE1 A:HIS145 3.1 2.0 1.0 CG A:HIS84 3.1 2.0 1.0 CE1 A:HIS82 3.3 2.0 1.0 CB A:HIS84 3.5 2.0 1.0 C11 A:061250 3.7 12.4 1.0 N1 A:061250 3.7 12.7 1.0 OD1 A:ASP86 3.8 2.0 1.0 SG A:CYS164 4.0 2.0 1.0 OD2 A:ASP86 4.0 2.0 1.0 CG A:HIS82 4.1 2.0 1.0 NE2 A:HIS84 4.1 2.0 1.0 ND1 A:HIS145 4.2 2.0 1.0 CG A:HIS145 4.2 2.0 1.0 CD2 A:HIS84 4.2 2.0 1.0 ND1 A:HIS82 4.2 2.0 1.0 C5 A:061250 4.3 12.4 1.0 CB A:CYS164 4.3 2.0 1.0 CG A:ASP86 4.3 2.0 1.0 C6 A:061250 4.4 12.2 1.0 N2 A:061250 4.6 12.2 1.0 C10 A:061250 4.6 12.1 1.0 NE2 A:HIS206 4.9 2.9 1.0 CA A:HIS84 4.9 2.0 1.0

Zinc binding site 2 out of 4 in the Metallo-Beta-Lactamase in Complex with L-159,061


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Metallo-Beta-Lactamase in Complex with L-159,061 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn252 b:7.4 occ:1.00 NE2 A:HIS206 2.1 2.9 1.0 OD2 A:ASP86 2.1 2.0 1.0 SG A:CYS164 2.3 2.0 1.0 N1 A:061250 2.4 12.7 1.0 ZN A:ZN251 2.8 2.0 1.0 CE1 A:HIS206 3.0 2.7 1.0 CG A:ASP86 3.2 2.0 1.0 CD2 A:HIS206 3.2 3.0 1.0 C5 A:061250 3.3 12.4 1.0 N2 A:061250 3.3 12.2 1.0 NE2 A:HIS145 3.4 2.0 1.0 OD1 A:ASP86 3.5 2.0 1.0 CB A:CYS164 3.6 2.0 1.0 C6 A:061250 3.8 12.2 1.0 NE2 A:HIS82 3.8 2.0 1.0 C11 A:061250 3.8 12.4 1.0 CE1 A:HIS145 3.9 2.0 1.0 ND1 A:HIS206 4.1 3.4 1.0 CE1 A:HIS82 4.3 2.0 1.0 CG A:HIS206 4.3 2.9 1.0 CD2 A:HIS145 4.3 2.0 1.0 N3 A:061250 4.4 12.7 1.0 CB A:ASP86 4.4 2.0 1.0 N4 A:061250 4.5 12.5 1.0 ND1 A:HIS84 4.7 2.0 1.0 O A:GLY205 4.8 2.3 1.0 C7 A:061250 4.9 12.3 1.0 CA A:CYS164 4.9 2.0 1.0 ND1 A:HIS145 4.9 2.0 1.0 C10 A:061250 4.9 12.1 1.0

Zinc binding site 3 out of 4 in the Metallo-Beta-Lactamase in Complex with L-159,061


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Metallo-Beta-Lactamase in Complex with L-159,061 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn251 b:11.7 occ:1.00 NE2 B:HIS82 1.8 2.0 1.0 ND1 B:HIS84 1.9 2.0 1.0 NE2 B:HIS145 2.1 7.9 1.0 CE1 B:HIS82 2.6 2.0 1.0 CD2 B:HIS145 2.7 7.2 1.0 CE1 B:HIS84 2.9 2.0 1.0 CG B:HIS84 2.9 2.0 1.0 CD2 B:HIS82 2.9 2.0 1.0 CE1 B:HIS145 3.2 8.0 1.0 ZN B:ZN252 3.2 34.2 1.0 CB B:HIS84 3.3 2.0 1.0 ND1 B:HIS82 3.7 2.0 1.0 CG B:HIS82 3.9 2.0 1.0 CG B:HIS145 3.9 7.0 1.0 NE2 B:HIS84 4.0 2.0 1.0 CD2 B:HIS84 4.0 2.0 1.0 OD1 B:ASP86 4.0 3.3 1.0 ND1 B:HIS145 4.1 8.0 1.0 SG B:CYS164 4.2 8.5 1.0 CB B:CYS164 4.5 5.8 1.0 CA B:HIS84 4.7 2.0 1.0 CB B:ALA146 4.7 6.8 1.0 SG B:CYS87 4.9 8.2 1.0 CG B:ASP86 4.9 3.1 1.0 OD2 B:ASP86 5.0 3.2 1.0

Zinc binding site 4 out of 4 in the Metallo-Beta-Lactamase in Complex with L-159,061


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Metallo-Beta-Lactamase in Complex with L-159,061 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn252 b:34.2 occ:1.00 SG B:CYS164 2.3 8.5 1.0 OD2 B:ASP86 3.1 3.2 1.0 NE2 B:HIS206 3.1 2.0 1.0 CB B:CYS164 3.2 5.8 1.0 OD1 B:ASP86 3.2 3.3 1.0 ZN B:ZN251 3.2 11.7 1.0 CD2 B:HIS206 3.4 2.0 1.0 CG B:ASP86 3.5 3.1 1.0 NE2 B:HIS145 3.6 7.9 1.0 CE1 B:HIS82 3.8 2.0 1.0 NE2 B:HIS82 4.1 2.0 1.0 CD2 B:HIS145 4.1 7.2 1.0 CE1 B:HIS206 4.2 2.0 1.0 CE1 B:HIS145 4.5 8.0 1.0 O B:HOH259 4.6 2.0 1.0 CA B:CYS164 4.6 4.5 1.0 CG B:HIS206 4.6 2.0 1.0 ND1 B:HIS84 4.9 2.0 1.0 CB B:ASP86 5.0 2.9 1.0

J.H.Toney, P.M.Fitzgerald, N.Grover-Sharma, S.H.Olson, W.J.May, J.G.Sundelof, D.E.Vanderwall, K.A.Cleary, S.K.Grant, J.K.Wu, J.W.Kozarich, D.L.Pompliano, G.G.Hammond. Antibiotic Sensitization Using Biphenyl Tetrazoles As Potent Inhibitors of Bacteroides Fragilis Metallo-Beta-Lactamase. Chem.Biol. V. 5 185 1998.
ISSN: ISSN 1074-5521
PubMed: 9545432
DOI: 10.1016/S1074-5521(98)90632-9